CATH Classification

Domain Context

CATH Clusters

Superfamily 3.30.1490.70
Functional Family

Enzyme Information

6.5.1.2
DNA ligase (NAD(+)).
based on mapping to UniProt P43813
NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + beta- nicotinamide D-nucleotide.
-!- The enzyme, typically found in bacteria, catalyzes the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA. -!- Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by NAD(+), forming a phosphoramide bond between adenylate and a lysine residue. -!- The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-(DNA). -!- Finally, the enzyme catalyzes a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate. -!- RNA can also act as substrate, to some extent. -!- Cf. EC 6.5.1.1, EC 6.5.1.6 and EC 6.5.1.7.

UniProtKB Entries (1)

P43813
DNLJ_HAEIN
Haemophilus influenzae Rd KW20
DNA ligase

PDB Structure

PDB 3PN1
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Novel Bacterial NAD+-Dependent DNA Ligase Inhibitors with Broad-Spectrum Activity and Antibacterial Efficacy In Vivo.
Mills, S.D., Eakin, A.E., Buurman, E.T., Newman, J.V., Gao, N., Huynh, H., Johnson, K.D., Lahiri, S., Shapiro, A.B., Walkup, G.K., Yang, W., Stokes, S.S.
Antimicrob.Agents Chemother.